ArticleBioMed research international2015
Tropomyosin and Actin Identified as Major Allergens of the Carpet Clam (Paphia textile) and the Effect of Cooking on Their Allergenicity.
Article in BioMed research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Serological Cross-Reactivity and Potential Allergenic Risk of Edible Cricket Proteins in Children and Adolescents with House Dust Mite Allergy.Journal of agricultural and food chemistry · 2026Article
- Fructose biphosphate aldolase: A new cassava allergen.The World Allergy Organization journal · 2023Article
- IgE-Mediated Shellfish Allergy in Children.Nutrients · 2023Review
- Allergenicity assessment ofHeliyon · 2021Article
- Survey of IgE Reactivity to Nonbiting Midges in Korea and Identification of IgE-Binding Protein.Allergy, asthma & immunology research · 2019Article
- Consumer-friendly food allergen detection: moving towards smartphone-based immunoassays.Analytical and bioanalytical chemistry · 2018Review
- Clinical and immuno-proteomic approach on Lantana camara pollen allergy-a major health hazard.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2016Article
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Authors and funding
5 authors.
Funding
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Abstract
objectivesTo identify the major allergenic proteins of clam (Paphia textile) and to investigate the effect of different cooking methods on the allergenicity of these identified proteins.
methodsClam protein extracts were separated by denaturing polyacrylamide gel electrophoresis. IgE reactive proteins were then analyzed by immunoblotting with sera from patients with positive skin prick tests (SPT) to the raw clam extract. Mass spectrometry was used to identify the major allergenic proteins of this clam.
resultsRaw extract showed 12 protein bands (18-150 kDa). In contrast, fewer protein bands were seen in the boiled extract; those ranging from 40 to 150 kDa were denatured. The protein profiles were similarly altered by frying or roasting. The immunoblots of raw and boiled extracts yielded 10 and 2 IgE-binding proteins, respectively. The fried and roasted extracts showed only a single IgE-binding protein at 37 kDa. Mass spectrometry analysis of the 37 and 42 kDa major allergens indicated that these spots were tropomyosin and actin, respectively.
conclusionThe two major allergens of Paphia textile were identified as the thermostable tropomyosin and a new thermolabile allergen actin.
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